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@article{1075200,
author = {Kosztyu, Pavlína and Cetkovská, Kateřina and Vousden, Karen H. and Uldrijan, Stjepan},
article_location = {Netherlands},
article_number = {16},
doi = {http://dx.doi.org/10.1016/j.febslet.2012.05.034},
keywords = {p53 degradation; Mdm2; Acidic domain; Mutagenesis; Ubiquitin ligase activity; Binding partner},
language = {eng},
issn = {0014-5793},
journal = {FEBS Letters},
title = {Mutational analysis reveals a dual role of Mdm2 acidic domain in the regulation of p53 stability},
volume = {586},
year = {2012}
}
TY - JOUR
ID - 1075200
AU - Kosztyu, Pavlína - Cetkovská, Kateřina - Vousden, Karen H. - Uldrijan, Stjepan
PY - 2012
TI - Mutational analysis reveals a dual role of Mdm2 acidic domain in the regulation of p53 stability
JF - FEBS Letters
VL - 586
IS - 16
SP - 2225-2231
EP - 2225-2231
PB - ELSEVIER SCIENCE BV
SN - 00145793
KW - p53 degradation
KW - Mdm2
KW - Acidic domain
KW - Mutagenesis
KW - Ubiquitin ligase activity
KW - Binding partner
N2 - The exact role of the central acidic domain of Mdm2 in p53 degradation remains unclear. We therefore performed a systematic and comprehensive analysis of the acidic domain using a series of short deletions and found that only a minor part of the domain was indispensable for Mdm2-mediated p53 ubiquitylation. Moreover, we identified a short stretch of acidic amino acids required for p53 degradation but not ubiquitylation, indicating that, in addition to p53 ubiquitylation, the acidic domain might be involved in a critical post-ubiquitylation step in p53 degradation. Rather than representing a single functional domain, different parts of the acidic region perform separate functions in p53 degradation, suggesting that it might be possible to therapeutically target them independently.
ER -
KOSZTYU, Pavlína, Kateřina CETKOVSKÁ, Karen H. VOUSDEN a Stjepan ULDRIJAN. Mutational analysis reveals a dual role of Mdm2 acidic domain in the regulation of p53 stability. \textit{FEBS Letters}. Netherlands: ELSEVIER SCIENCE BV, 2012, roč.~586, č.~16, s.~2225-2231. ISSN~0014-5793. doi:10.1016/j.febslet.2012.05.034.
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